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Database: PDB
Entry: 6DED
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HEADER    ENDOCYTOSIS                             11-MAY-18   6DED              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINAL ARM DOMAIN OF HOMO SAPIENS SPIN90 
TITLE    2 (SH3-PROTEIN INTERACTING WITH NCK), RESIDUES 351-722                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NCK-INTERACTING PROTEIN WITH SH3 DOMAIN;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 350-722;                                      
COMPND   5 SYNONYM: 54 KDA VACA-INTERACTING PROTEIN, 54 KDA VIMENTIN-INTERACTING
COMPND   6 PROTEIN, VIP54, 90 KDA SH3 PROTEIN INTERACTING WITH NCK, AF3P21, DIA-
COMPND   7 INTERACTING PROTEIN 1, DIP-1, DIAPHANOUS PROTEIN-INTERACTING PROTEIN,
COMPND   8 SH3 ADAPTER PROTEIN SPIN90, WASP-INTERACTING SH3-DOMAIN PROTEIN,     
COMPND   9 WISH, WISKOTT-ALDRICH SYNDROME PROTEIN-INTERACTING PROTEIN;          
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NCKIPSD, AF3P21, SPIN90;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGV67                                     
KEYWDS    INACTIVE FORM, N-TERMINALLY TRUNCATED SPIN90, 6 AND 2-3 ARMADILLO     
KEYWDS   2 REPEATS, UNABLE TO ACTIVATE ARP2-3 COMPLEX, ENDOCYTOSIS              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.NOLEN,Q.LUAN                                                      
REVDAT   4   01-JAN-20 6DED    1       REMARK                                   
REVDAT   3   28-NOV-18 6DED    1       JRNL                                     
REVDAT   2   31-OCT-18 6DED    1       JRNL                                     
REVDAT   1   24-OCT-18 6DED    0                                                
JRNL        AUTH   Q.LUAN,S.L.LIU,L.A.HELGESON,B.J.NOLEN                        
JRNL        TITL   STRUCTURE OF THE NUCLEATION-PROMOTING FACTOR SPIN90 BOUND TO 
JRNL        TITL 2 THE ACTIN FILAMENT NUCLEATOR ARP2/3 COMPLEX.                 
JRNL        REF    EMBO J.                       V.  37       2018              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   30322896                                                     
JRNL        DOI    10.15252/EMBJ.2018100005                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 52992                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.830                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2559                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.7034 -  5.7684    0.95     2768   150  0.1956 0.2230        
REMARK   3     2  5.7684 -  4.5816    1.00     2866   138  0.1966 0.2129        
REMARK   3     3  4.5816 -  4.0033    0.99     2817   142  0.1767 0.1985        
REMARK   3     4  4.0033 -  3.6377    0.99     2801   165  0.1870 0.2076        
REMARK   3     5  3.6377 -  3.3772    1.00     2817   171  0.1915 0.2085        
REMARK   3     6  3.3772 -  3.1782    1.00     2774   171  0.2144 0.2407        
REMARK   3     7  3.1782 -  3.0191    1.00     2827   151  0.2230 0.2451        
REMARK   3     8  3.0191 -  2.8878    1.00     2846   116  0.2270 0.2561        
REMARK   3     9  2.8878 -  2.7766    1.00     2824   133  0.2293 0.2460        
REMARK   3    10  2.7766 -  2.6808    1.00     2826   148  0.2362 0.2638        
REMARK   3    11  2.6808 -  2.5971    1.00     2797   149  0.2445 0.2725        
REMARK   3    12  2.5971 -  2.5228    1.00     2835   125  0.2507 0.3029        
REMARK   3    13  2.5228 -  2.4564    1.00     2777   146  0.2548 0.2979        
REMARK   3    14  2.4564 -  2.3965    0.99     2774   164  0.2663 0.3088        
REMARK   3    15  2.3965 -  2.3420    0.99     2834   114  0.2695 0.3449        
REMARK   3    16  2.3420 -  2.2922    0.99     2803   122  0.2913 0.3435        
REMARK   3    17  2.2922 -  2.2464    1.00     2766   140  0.2963 0.3149        
REMARK   3    18  2.2464 -  2.2040    0.93     2681   114  0.3274 0.4105        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5468                                  
REMARK   3   ANGLE     :  0.595           7413                                  
REMARK   3   CHIRALITY :  0.022            868                                  
REMARK   3   PLANARITY :  0.003            948                                  
REMARK   3   DIHEDRAL  : 12.327           2037                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2927   7.3402 -23.7301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2548 T22:   0.2370                                     
REMARK   3      T33:   0.2657 T12:  -0.0145                                     
REMARK   3      T13:   0.0265 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4259 L22:   0.2530                                     
REMARK   3      L33:   0.5256 L12:  -0.0257                                     
REMARK   3      L13:   0.3828 L23:  -0.1799                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0434 S12:   0.0309 S13:   0.0196                       
REMARK   3      S21:  -0.0191 S22:   0.0078 S23:  -0.0293                       
REMARK   3      S31:  -0.0168 S32:   0.0084 S33:   0.0354                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6DED COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234280.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797423                          
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : SAGITALLY FOCUSING 2ND CRYSTAL     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000 2.3.10                    
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000 2.3.10                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53032                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: SAD MODEL                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS, PH 7.5, 700 MM SODIUM        
REMARK 280  POTASSIUM TARTRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       38.08500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   350                                                      
REMARK 465     PRO A   351                                                      
REMARK 465     VAL A   352                                                      
REMARK 465     MET A   353                                                      
REMARK 465     GLU A   354                                                      
REMARK 465     GLN A   355                                                      
REMARK 465     VAL A   356                                                      
REMARK 465     LEU A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     SER A   359                                                      
REMARK 465     LEU A   360                                                      
REMARK 465     VAL A   361                                                      
REMARK 465     GLU A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     LYS A   364                                                      
REMARK 465     ASP A   365                                                      
REMARK 465     LEU A   366                                                      
REMARK 465     SER A   367                                                      
REMARK 465     MET A   368                                                      
REMARK 465     ALA A   369                                                      
REMARK 465     LEU A   370                                                      
REMARK 465     PRO A   371                                                      
REMARK 465     SER A   372                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     GLN A   374                                                      
REMARK 465     VAL A   375                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     LYS A   393                                                      
REMARK 465     ASP A   394                                                      
REMARK 465     ASP A   395                                                      
REMARK 465     ALA A   396                                                      
REMARK 465     LEU A   544                                                      
REMARK 465     ASP A   545                                                      
REMARK 465     THR A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     PRO A   721                                                      
REMARK 465     SER A   722                                                      
REMARK 465     SER B   350                                                      
REMARK 465     PRO B   351                                                      
REMARK 465     VAL B   352                                                      
REMARK 465     MET B   353                                                      
REMARK 465     GLU B   354                                                      
REMARK 465     GLN B   355                                                      
REMARK 465     VAL B   356                                                      
REMARK 465     LEU B   357                                                      
REMARK 465     LEU B   358                                                      
REMARK 465     SER B   359                                                      
REMARK 465     LEU B   360                                                      
REMARK 465     VAL B   361                                                      
REMARK 465     GLU B   362                                                      
REMARK 465     GLY B   363                                                      
REMARK 465     LYS B   364                                                      
REMARK 465     ASP B   365                                                      
REMARK 465     LEU B   366                                                      
REMARK 465     SER B   367                                                      
REMARK 465     MET B   368                                                      
REMARK 465     ALA B   369                                                      
REMARK 465     LEU B   370                                                      
REMARK 465     PRO B   371                                                      
REMARK 465     SER B   372                                                      
REMARK 465     GLY B   373                                                      
REMARK 465     GLN B   374                                                      
REMARK 465     VAL B   375                                                      
REMARK 465     ASP B   395                                                      
REMARK 465     ALA B   396                                                      
REMARK 465     SER B   722                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 388    CG   OD1  OD2                                       
REMARK 470     ARG A 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 398    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 437    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 548    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 569    CG   OD1  OD2                                       
REMARK 470     GLU A 588    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 393    CG   CD   CE   NZ                                   
REMARK 470     ASP B 394    CG   OD1  OD2                                       
REMARK 470     GLN B 398    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 496    CG   CD   OE1  NE2                                  
REMARK 470     PRO B 543    CG   CD                                             
REMARK 470     LEU B 544    CG   CD1  CD2                                       
REMARK 470     ASP B 545    CG   OD1  OD2                                       
REMARK 470     THR B 546    OG1  CG2                                            
REMARK 470     THR B 547    OG1  CG2                                            
REMARK 470     GLU B 548    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 569    CG   OD1  OD2                                       
REMARK 470     ARG B 596    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 494       50.04   -111.66                                   
REMARK 500    ASP B 494       50.02   -111.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 948        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 949        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH A 950        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH B 971        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B 972        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH B 973        DISTANCE =  7.11 ANGSTROMS                       
DBREF  6DED A  350   722  UNP    Q9NZQ3   SPN90_HUMAN    350    722             
DBREF  6DED B  350   722  UNP    Q9NZQ3   SPN90_HUMAN    350    722             
SEQRES   1 A  373  SER PRO VAL MET GLU GLN VAL LEU LEU SER LEU VAL GLU          
SEQRES   2 A  373  GLY LYS ASP LEU SER MET ALA LEU PRO SER GLY GLN VAL          
SEQRES   3 A  373  CYS HIS ASP GLN GLN ARG LEU GLU VAL ILE PHE ALA ASP          
SEQRES   4 A  373  LEU ALA ARG ARG LYS ASP ASP ALA GLN GLN ARG SER TRP          
SEQRES   5 A  373  ALA LEU TYR GLU ASP GLU GLY VAL ILE ARG CYS TYR LEU          
SEQRES   6 A  373  GLU GLU LEU LEU HIS ILE LEU THR ASP ALA ASP PRO GLU          
SEQRES   7 A  373  VAL CYS LYS LYS MET CYS LYS ARG ASN GLU PHE GLU SER          
SEQRES   8 A  373  VAL LEU ALA LEU VAL ALA TYR TYR GLN MET GLU HIS ARG          
SEQRES   9 A  373  ALA SER LEU ARG LEU LEU LEU LEU LYS CYS PHE GLY ALA          
SEQRES  10 A  373  MET CYS SER LEU ASP ALA ALA ILE ILE SER THR LEU VAL          
SEQRES  11 A  373  SER SER VAL LEU PRO VAL GLU LEU ALA ARG ASP MET GLN          
SEQRES  12 A  373  THR ASP THR GLN ASP HIS GLN LYS LEU CYS TYR SER ALA          
SEQRES  13 A  373  LEU ILE LEU ALA MET VAL PHE SER MET GLY GLU ALA VAL          
SEQRES  14 A  373  PRO TYR ALA HIS TYR GLU HIS LEU GLY THR PRO PHE ALA          
SEQRES  15 A  373  GLN PHE LEU LEU ASN ILE VAL GLU ASP GLY LEU PRO LEU          
SEQRES  16 A  373  ASP THR THR GLU GLN LEU PRO ASP LEU CYS VAL ASN LEU          
SEQRES  17 A  373  LEU LEU ALA LEU ASN LEU HIS LEU PRO ALA ALA ASP GLN          
SEQRES  18 A  373  ASN VAL ILE MET ALA ALA LEU SER LYS HIS ALA ASN VAL          
SEQRES  19 A  373  LYS ILE PHE SER GLU LYS LEU LEU LEU LEU LEU ASN ARG          
SEQRES  20 A  373  GLY ASP ASP PRO VAL ARG ILE PHE LYS HIS GLU PRO GLN          
SEQRES  21 A  373  PRO PRO HIS SER VAL LEU LYS PHE LEU GLN ASP VAL PHE          
SEQRES  22 A  373  GLY SER PRO ALA THR ALA ALA ILE PHE TYR HIS THR ASP          
SEQRES  23 A  373  MET MET ALA LEU ILE ASP ILE THR VAL ARG HIS ILE ALA          
SEQRES  24 A  373  ASP LEU SER PRO GLY ASP LYS LEU ARG MET GLU TYR LEU          
SEQRES  25 A  373  SER LEU MET HIS ALA ILE VAL ARG THR THR PRO TYR LEU          
SEQRES  26 A  373  GLN HIS ARG HIS ARG LEU PRO ASP LEU GLN ALA ILE LEU          
SEQRES  27 A  373  ARG ARG ILE LEU ASN GLU GLU GLU THR SER PRO GLN CYS          
SEQRES  28 A  373  GLN MET ASP ARG MET ILE VAL ARG GLU MET CYS LYS GLU          
SEQRES  29 A  373  PHE LEU VAL LEU GLY GLU ALA PRO SER                          
SEQRES   1 B  373  SER PRO VAL MET GLU GLN VAL LEU LEU SER LEU VAL GLU          
SEQRES   2 B  373  GLY LYS ASP LEU SER MET ALA LEU PRO SER GLY GLN VAL          
SEQRES   3 B  373  CYS HIS ASP GLN GLN ARG LEU GLU VAL ILE PHE ALA ASP          
SEQRES   4 B  373  LEU ALA ARG ARG LYS ASP ASP ALA GLN GLN ARG SER TRP          
SEQRES   5 B  373  ALA LEU TYR GLU ASP GLU GLY VAL ILE ARG CYS TYR LEU          
SEQRES   6 B  373  GLU GLU LEU LEU HIS ILE LEU THR ASP ALA ASP PRO GLU          
SEQRES   7 B  373  VAL CYS LYS LYS MET CYS LYS ARG ASN GLU PHE GLU SER          
SEQRES   8 B  373  VAL LEU ALA LEU VAL ALA TYR TYR GLN MET GLU HIS ARG          
SEQRES   9 B  373  ALA SER LEU ARG LEU LEU LEU LEU LYS CYS PHE GLY ALA          
SEQRES  10 B  373  MET CYS SER LEU ASP ALA ALA ILE ILE SER THR LEU VAL          
SEQRES  11 B  373  SER SER VAL LEU PRO VAL GLU LEU ALA ARG ASP MET GLN          
SEQRES  12 B  373  THR ASP THR GLN ASP HIS GLN LYS LEU CYS TYR SER ALA          
SEQRES  13 B  373  LEU ILE LEU ALA MET VAL PHE SER MET GLY GLU ALA VAL          
SEQRES  14 B  373  PRO TYR ALA HIS TYR GLU HIS LEU GLY THR PRO PHE ALA          
SEQRES  15 B  373  GLN PHE LEU LEU ASN ILE VAL GLU ASP GLY LEU PRO LEU          
SEQRES  16 B  373  ASP THR THR GLU GLN LEU PRO ASP LEU CYS VAL ASN LEU          
SEQRES  17 B  373  LEU LEU ALA LEU ASN LEU HIS LEU PRO ALA ALA ASP GLN          
SEQRES  18 B  373  ASN VAL ILE MET ALA ALA LEU SER LYS HIS ALA ASN VAL          
SEQRES  19 B  373  LYS ILE PHE SER GLU LYS LEU LEU LEU LEU LEU ASN ARG          
SEQRES  20 B  373  GLY ASP ASP PRO VAL ARG ILE PHE LYS HIS GLU PRO GLN          
SEQRES  21 B  373  PRO PRO HIS SER VAL LEU LYS PHE LEU GLN ASP VAL PHE          
SEQRES  22 B  373  GLY SER PRO ALA THR ALA ALA ILE PHE TYR HIS THR ASP          
SEQRES  23 B  373  MET MET ALA LEU ILE ASP ILE THR VAL ARG HIS ILE ALA          
SEQRES  24 B  373  ASP LEU SER PRO GLY ASP LYS LEU ARG MET GLU TYR LEU          
SEQRES  25 B  373  SER LEU MET HIS ALA ILE VAL ARG THR THR PRO TYR LEU          
SEQRES  26 B  373  GLN HIS ARG HIS ARG LEU PRO ASP LEU GLN ALA ILE LEU          
SEQRES  27 B  373  ARG ARG ILE LEU ASN GLU GLU GLU THR SER PRO GLN CYS          
SEQRES  28 B  373  GLN MET ASP ARG MET ILE VAL ARG GLU MET CYS LYS GLU          
SEQRES  29 B  373  PHE LEU VAL LEU GLY GLU ALA PRO SER                          
FORMUL   3  HOH   *323(H2 O)                                                    
HELIX    1 AA1 CYS A  376  ARG A  391  1                                  16    
HELIX    2 AA2 SER A  400  GLU A  405  5                                   6    
HELIX    3 AA3 ASP A  406  ALA A  424  1                                  19    
HELIX    4 AA4 ASP A  425  GLU A  451  1                                  27    
HELIX    5 AA5 ARG A  453  ASP A  471  1                                  19    
HELIX    6 AA6 ASP A  471  SER A  481  1                                  11    
HELIX    7 AA7 VAL A  482  ASP A  494  1                                  13    
HELIX    8 AA8 ASP A  497  PHE A  512  1                                  16    
HELIX    9 AA9 PRO A  519  HIS A  525  5                                   7    
HELIX   10 AB1 GLY A  527  ASP A  540  1                                  14    
HELIX   11 AB2 GLN A  549  LEU A  563  1                                  15    
HELIX   12 AB3 ASN A  571  LYS A  579  1                                   9    
HELIX   13 AB4 VAL A  583  GLY A  597  1                                  15    
HELIX   14 AB5 HIS A  612  PHE A  622  1                                  11    
HELIX   15 AB6 SER A  624  ALA A  629  1                                   6    
HELIX   16 AB7 TYR A  632  LEU A  650  1                                  19    
HELIX   17 AB8 LEU A  656  THR A  671  1                                  16    
HELIX   18 AB9 PRO A  672  ARG A  677  1                                   6    
HELIX   19 AC1 ARG A  679  ASN A  692  1                                  14    
HELIX   20 AC2 SER A  697  PHE A  714  1                                  18    
HELIX   21 AC3 LEU A  715  GLY A  718  5                                   4    
HELIX   22 AC4 HIS B  377  ARG B  391  1                                  15    
HELIX   23 AC5 SER B  400  GLU B  405  5                                   6    
HELIX   24 AC6 ASP B  406  ALA B  424  1                                  19    
HELIX   25 AC7 ASP B  425  GLU B  451  1                                  27    
HELIX   26 AC8 ARG B  453  ASP B  471  1                                  19    
HELIX   27 AC9 ASP B  471  SER B  481  1                                  11    
HELIX   28 AD1 VAL B  482  ASP B  494  1                                  13    
HELIX   29 AD2 ASP B  497  PHE B  512  1                                  16    
HELIX   30 AD3 PRO B  519  HIS B  525  5                                   7    
HELIX   31 AD4 GLY B  527  ASP B  540  1                                  14    
HELIX   32 AD5 GLN B  549  LEU B  563  1                                  15    
HELIX   33 AD6 ASN B  571  LYS B  579  1                                   9    
HELIX   34 AD7 VAL B  583  GLY B  597  1                                  15    
HELIX   35 AD8 HIS B  612  PHE B  622  1                                  11    
HELIX   36 AD9 SER B  624  ALA B  629  1                                   6    
HELIX   37 AE1 TYR B  632  LEU B  650  1                                  19    
HELIX   38 AE2 LYS B  655  THR B  671  1                                  17    
HELIX   39 AE3 PRO B  672  ARG B  677  1                                   6    
HELIX   40 AE4 ARG B  679  ASN B  692  1                                  14    
HELIX   41 AE5 SER B  697  PHE B  714  1                                  18    
HELIX   42 AE6 LEU B  715  GLY B  718  5                                   4    
CISPEP   1 GLU A  607    PRO A  608          0         1.97                     
CISPEP   2 GLU B  607    PRO B  608          0         0.88                     
CRYST1   76.365   76.170   92.257  90.00  93.12  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013095  0.000000  0.000714        0.00000                         
SCALE2      0.000000  0.013129  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010855        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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